View source for 9jxl


==Cryo-EM structure of human XPR1 in an open state at the intracellular gate and a closed state at the extracellular gate, obtained through local refinement==
<StructureSection load='9jxl' size='340' side='right'caption='[[9jxl]], [[Resolution|resolution]] 3.23&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9jxl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9JXL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9JXL FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.23&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=9jxl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9jxl OCA], [https://pdbe.org/9jxl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9jxl RCSB], [https://www.ebi.ac.uk/pdbsum/9jxl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9jxl ProSAT]</span></td></tr>
</table>
== Disease ==
[https://www.uniprot.org/uniprot/S53A1_HUMAN S53A1_HUMAN] Bilateral striopallidodentate calcinosis. The disease is caused by variants affecting the gene represented in this entry.
== Function ==
[https://www.uniprot.org/uniprot/S53A1_HUMAN S53A1_HUMAN] Inorganic ion transporter that mediates phosphate ion export across plasma membrane. Plays a major role in phosphate homeostasis, preventing intracellular phosphate accumulation and possible calcium phosphate precipitation, ultimately preserving calcium signaling. The molecular mechanism of phosphate transport, whether electrogenic, electroneutral or coupled to other ions, remains to be elucidated (By similarity) (PubMed:23791524, PubMed:25938945, PubMed:31043717). Binds inositol hexakisphosphate (Ins6P) and similar inositol polyphosphates, such as 5-diphospho-inositol pentakisphosphate (5-InsP7), important intracellular signaling molecules involved in regulation of phosphate flux (PubMed:27080106).[UniProtKB:Q9Z0U0]<ref>PMID:23791524</ref> <ref>PMID:25938945</ref> <ref>PMID:27080106</ref> <ref>PMID:31043717</ref> 
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Bai Z]]
[[Category: Corry B]]
[[Category: Gu C]]
[[Category: Han Y]]
[[Category: Jessen H]]
[[Category: Jin R]]
[[Category: Lei M]]
[[Category: Shears S]]
[[Category: Sun Y]]
[[Category: Wallis C]]
[[Category: Wang H]]
[[Category: Wang X]]
[[Category: Zhang Y]]